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Article: Subunits of the translocon interact with components of the oligosaccharyl transferase complex

TitleSubunits of the translocon interact with components of the oligosaccharyl transferase complex
Authors
Issue Date2005
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2005, v. 280 n. 24, p. 22917-22924 How to Cite?
AbstractFollowing initiation of translocation across the membrane of the endoplasmic reticulum via the translocon, polypeptide chains are N-glycosylated by the oligosaccharyl transferase (OT) enzyme complex. Translocation and N-glycosylation are concurrent events and would be expected to require juxtaposition of the translocon and the OT complex. To determine whether any of the subunits of the OT complex and translocon mediate interactions between the two complexes, we initiated a systematic study in budding yeast using the split-ubiquitin approach. Interestingly, the OT subunit Stt3p was found to interact only with Sec61p, whereas another OT subunit, Ost4p, was found to interact with all three components of the translocon, Sec61p, Sbh1p, and Sss1p. The OT subunit Wbp1p was found to interact very strongly with Sec61p and Sbh1p and weakly with Sss1p. Other OT subunits, Ost1p, Ost2p, and Swp1p were found to interact with Sec61p and either Sbh1p or Sss1p. Ost3p exhibited a weak interaction with Sec61p and Sbh1p, whereas Ost5p and Ost6p interacted very weakly with Sec61p and failed to interact with Sbh1p or Sss1p. We were able to confirm these split-ubiquitin findings by a chemical cross-linking technique. Based on our findings using these two techniques, we conclude that the association of these two complexes is stabilized via multiple protein-protein contacts. Based on extrapolation of the structural parameters of the crystal structure of the prokaryotic Sec complex to the eukaryotic complex, we propose a working model to understand the organization of the translocon-OT supercomplex. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/178890
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChavan, Men_US
dc.contributor.authorYan, Aen_US
dc.contributor.authorLennarz, WJen_US
dc.date.accessioned2012-12-19T09:50:30Z-
dc.date.available2012-12-19T09:50:30Z-
dc.date.issued2005en_US
dc.identifier.citationJournal Of Biological Chemistry, 2005, v. 280 n. 24, p. 22917-22924en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/178890-
dc.description.abstractFollowing initiation of translocation across the membrane of the endoplasmic reticulum via the translocon, polypeptide chains are N-glycosylated by the oligosaccharyl transferase (OT) enzyme complex. Translocation and N-glycosylation are concurrent events and would be expected to require juxtaposition of the translocon and the OT complex. To determine whether any of the subunits of the OT complex and translocon mediate interactions between the two complexes, we initiated a systematic study in budding yeast using the split-ubiquitin approach. Interestingly, the OT subunit Stt3p was found to interact only with Sec61p, whereas another OT subunit, Ost4p, was found to interact with all three components of the translocon, Sec61p, Sbh1p, and Sss1p. The OT subunit Wbp1p was found to interact very strongly with Sec61p and Sbh1p and weakly with Sss1p. Other OT subunits, Ost1p, Ost2p, and Swp1p were found to interact with Sec61p and either Sbh1p or Sss1p. Ost3p exhibited a weak interaction with Sec61p and Sbh1p, whereas Ost5p and Ost6p interacted very weakly with Sec61p and failed to interact with Sbh1p or Sss1p. We were able to confirm these split-ubiquitin findings by a chemical cross-linking technique. Based on our findings using these two techniques, we conclude that the association of these two complexes is stabilized via multiple protein-protein contacts. Based on extrapolation of the structural parameters of the crystal structure of the prokaryotic Sec complex to the eukaryotic complex, we propose a working model to understand the organization of the translocon-OT supercomplex. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshCross-Linking Reagents - Pharmacologyen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshEndoplasmic Reticulum - Metabolismen_US
dc.subject.meshGalactosidases - Metabolismen_US
dc.subject.meshGenotypeen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHexosyltransferases - Chemistry - Metabolismen_US
dc.subject.meshMembrane Proteins - Chemistry - Metabolismen_US
dc.subject.meshMembrane Transport Proteinsen_US
dc.subject.meshModels, Biologicalen_US
dc.subject.meshPeptides - Chemistryen_US
dc.subject.meshPlasmids - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshProtein Transporten_US
dc.subject.meshSaccharomyces Cerevisiae Proteins - Chemistry - Metabolismen_US
dc.subject.meshSaccharomycetales - Metabolismen_US
dc.subject.meshUbiquitin - Metabolismen_US
dc.subject.meshVesicular Transport Proteinsen_US
dc.titleSubunits of the translocon interact with components of the oligosaccharyl transferase complexen_US
dc.typeArticleen_US
dc.identifier.emailYan, A: ayan8@hku.hken_US
dc.identifier.authorityYan, A=rp00823en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M502858200en_US
dc.identifier.pmid15831493-
dc.identifier.scopuseid_2-s2.0-20744441520en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-20744441520&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume280en_US
dc.identifier.issue24en_US
dc.identifier.spage22917en_US
dc.identifier.epage22924en_US
dc.identifier.isiWOS:000229741800045-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChavan, M=6601963205en_US
dc.identifier.scopusauthoridYan, A=8621667000en_US
dc.identifier.scopusauthoridLennarz, WJ=7101750236en_US

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